GID4_MOUSE
ID GID4_MOUSE Reviewed; 217 AA.
AC Q9CPY6; Q3TP79; Q7TT31; Q99JE9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glucose-induced degradation protein 4 homolog;
DE AltName: Full=Vacuolar import and degradation protein 24 homolog;
GN Name=Gid4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Spinal cord, Stomach, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-217.
RC TISSUE=Skeletal muscle;
RA Ievolella C., Zara I., Millino C., Faulkner G., Lanfranchi G.;
RT "Full length sequencing of some human and murine muscular transcripts
RT (Telethon Italy project B41).";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Substrate-recognition subunit of the CTLH E3 ubiquitin-
CC protein ligase complex that selectively accepts ubiquitin from UBE2H
CC and mediates ubiquitination and subsequent proteasomal degradation of
CC the transcription factor HBP1. Binds proteins and peptides with a
CC Pro/N-degron consisting of an unmodified N-terminal Pro followed by a
CC small residue, and has the highest affinity for the peptide Pro-Gly-
CC Leu-Trp. Binds peptides with an N-terminal sequence of the type Pro-
CC [Ala,Gly]-[Leu,Met,Gln,Ser,Tyr]-[Glu,Gly,His,Ser,Val,Trp,Tyr]. Does not
CC bind peptides with an acetylated N-terminal Pro residue.
CC {ECO:0000250|UniProtKB:Q8IVV7}.
CC -!- SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9
CC and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog
CC RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA,
CC RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9
CC and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and
CC YPEL5 have ancillary roles. {ECO:0000250|UniProtKB:Q8IVV7}.
CC -!- DOMAIN: The first four residues of target peptides with a free N-
CC terminal Pro (a Pro/N-degron) are bound inside a deep and narrow beta-
CC barrel structure. {ECO:0000250|UniProtKB:Q8IVV7}.
CC -!- SIMILARITY: Belongs to the GID4/VID24 family. {ECO:0000305}.
CC -!- CAUTION: The human orthologous sequence is longer in the N-terminus.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC34590.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK012042; BAB27989.1; -; mRNA.
DR EMBL; AK017120; BAB30608.1; -; mRNA.
DR EMBL; AK039435; BAC30346.1; -; mRNA.
DR EMBL; AK077759; BAC36995.1; -; mRNA.
DR EMBL; AK142753; BAE25186.1; -; mRNA.
DR EMBL; AK164644; BAE37858.1; -; mRNA.
DR EMBL; AL596090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044901; AAH44901.1; -; mRNA.
DR EMBL; BC046821; AAH46821.1; -; mRNA.
DR EMBL; BC052418; AAH52418.1; -; mRNA.
DR EMBL; AJ404329; CAC34590.1; ALT_SEQ; mRNA.
DR CCDS; CCDS24790.1; -.
DR RefSeq; NP_080033.3; NM_025757.4.
DR AlphaFoldDB; Q9CPY6; -.
DR SMR; Q9CPY6; -.
DR STRING; 10090.ENSMUSP00000064926; -.
DR PhosphoSitePlus; Q9CPY6; -.
DR EPD; Q9CPY6; -.
DR MaxQB; Q9CPY6; -.
DR PaxDb; Q9CPY6; -.
DR PeptideAtlas; Q9CPY6; -.
DR PRIDE; Q9CPY6; -.
DR ProteomicsDB; 265745; -.
DR Antibodypedia; 25602; 88 antibodies from 18 providers.
DR DNASU; 66771; -.
DR Ensembl; ENSMUST00000070681; ENSMUSP00000064926; ENSMUSG00000018415.
DR Ensembl; ENSMUST00000139477; ENSMUSP00000135441; ENSMUSG00000018415.
DR GeneID; 66771; -.
DR KEGG; mmu:66771; -.
DR UCSC; uc007jfw.2; mouse.
DR CTD; 79018; -.
DR MGI; MGI:1914021; Gid4.
DR VEuPathDB; HostDB:ENSMUSG00000018415; -.
DR eggNOG; KOG4635; Eukaryota.
DR GeneTree; ENSGT00500000044930; -.
DR HOGENOM; CLU_028759_2_0_1; -.
DR InParanoid; Q9CPY6; -.
DR OMA; KHWGQFL; -.
DR OrthoDB; 1254963at2759; -.
DR PhylomeDB; Q9CPY6; -.
DR TreeFam; TF323749; -.
DR BioGRID-ORCS; 66771; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Gid4; mouse.
DR PRO; PR:Q9CPY6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CPY6; protein.
DR Bgee; ENSMUSG00000018415; Expressed in interventricular septum and 240 other tissues.
DR Genevisible; Q9CPY6; MM.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR018618; Vacuolar_import/degrad_Vid24.
DR Pfam; PF09783; Vac_ImportDeg; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..217
FT /note="Glucose-induced degradation protein 4 homolog"
FT /id="PRO_0000079303"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 49
FT /note="Interaction with the N-terminal Pro (Pro/N-degron)
FT of proteins that are targeted for degradation"
FT /evidence="ECO:0000250|UniProtKB:Q8IVV7"
FT SITE 154
FT /note="Interaction with the N-terminal Pro (Pro/N-degron)
FT of proteins that are targeted for degradation"
FT /evidence="ECO:0000250|UniProtKB:Q8IVV7"
FT SITE 175
FT /note="Interaction with the N-terminal Pro (Pro/N-degron)
FT of proteins that are targeted for degradation"
FT /evidence="ECO:0000250|UniProtKB:Q8IVV7"
FT CONFLICT 130
FT /note="K -> E (in Ref. 3; AAH52418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 24863 MW; E6FFA722A0E67043 CRC64;
MPVRTECPPP AGASTTSAAS LIPPPPINTQ QPGVATSLLY SGSKFRGHQK SKGNSYDVEV
VLQHVDTGNS YLCGYLKIKG LTEEYPTLTT FFEGEIISKK HPFLTRKWDA DEDVDRKHWG
KFLAFYQYAK SFNSDDFDYE ELKNGDYVFM RWKEQFLVPD HTIKDISGAS FAGFYYICFQ
KSAASIEGYY YHRSSEWYQS LNLTHVPEHS APIYEFR
